A0A0G2K1Q8 · ABCA3_RAT
- ProteinPhospholipid-transporting ATPase ABCA3
- GeneAbca3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1704 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the ATP-dependent transport of phospholipids such as phosphatidylcholine and phosphoglycerol from the cytoplasm into the lumen side of lamellar bodies, in turn participates in the lamellar bodies biogenesis and homeostasis of pulmonary surfactant. Transports preferentially phosphatidylcholine containing short acyl chains. In addition plays a role as an efflux transporter of miltefosine across macrophage membranes and free cholesterol (FC) through intralumenal vesicles by removing FC from the cell as a component of surfactant and protects cells from free cholesterol toxicity.
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine(in) + ATP + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine(out) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
- ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H+ + phosphateThis reaction proceeds in the forward direction.
- 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)(in) + ATP + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)(out) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
Features
Showing features for site, binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhospholipid-transporting ATPase ABCA3
- EC number
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionA0A0G2K1Q8
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endosome, multivesicular body membrane ; Multi-pass membrane protein
Note: Localized in the limiting membrane of lamellar bodies in lung alveolar type II cells. Trafficks via the Golgi, sorting vesicles (SVs) and late endosome/multivesicular body network directly to the outer membrane of lamellar bodies in AT2 lung epithelial cells or to lysosomes and lysosomal-related organelles (LROs) in other cells where undergoes proteolytic cleavage and oligosaccharide processing from high mannose type to complex type. Oligomers formation takes place in a post-endoplasmic reticulum compartment.
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 22-42 | Helical | ||||
Sequence: VLVTVLELFLPLLFSGILIWL | ||||||
Transmembrane | 251-271 | Helical | ||||
Sequence: ISDPFLIAIQYQLPLLLMLSF | ||||||
Transmembrane | 307-327 | Helical | ||||
Sequence: AWFLMFLLFSLIVVSFMTLLF | ||||||
Transmembrane | 344-364 | Helical | ||||
Sequence: SLVLAFLLCFAISSISFSFMV | ||||||
Transmembrane | 373-393 | Helical | ||||
Sequence: MAATVGGFLYFFTYTPYFFVA | ||||||
Transmembrane | 405-425 | Helical | ||||
Sequence: LLSCLLSNVAMAMGAQLIGKF | ||||||
Transmembrane | 1100-1120 | Helical | ||||
Sequence: IALNLLIAMAFLASTFSILAV | ||||||
Transmembrane | 1144-1164 | Helical | ||||
Sequence: SALLWDLISFLVPSLLLLVVF | ||||||
Transmembrane | 1183-1203 | Helical | ||||
Sequence: LLLMLYGWAIIPLMYLLSFFF | ||||||
Transmembrane | 1213-1233 | Helical | ||||
Sequence: LTIFNILSGIATFIVVTIMRI | ||||||
Transmembrane | 1245-1265 | Helical | ||||
Sequence: LDHVFLVLPNHCLGMAVSNFY | ||||||
Transmembrane | 1310-1330 | Helical | ||||
Sequence: MAASGGIYLTLLFLIETNLLW |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000452299 | 1-1704 | Phospholipid-transporting ATPase ABCA3 | |||
Sequence: MVVLRQLRLLLWKNYTLKKRKVLVTVLELFLPLLFSGILIWLRLKIQSENVPNATVYPDQHIQELPLFFSFPPPGGSWELAYVPSHSDAARTITEAVRREFMIKMRVHGFSSEKDFEDYVRYDNHSSNVLAAVVFEHTFNHSKDPLPLAVRYHLRFSYTRRNYMWTQTGNLFLKETEGWHTASLFPLFPSPGPREPSSPDGGEPGYIREGFLAVQHAVDKAIMHYHANASAHQLFQKLTVITKRFPFPPYISDPFLIAIQYQLPLLLMLSFTYTSLTIIRAVVQEKEKKLKEYMRMMGLSSWLHWSAWFLMFLLFSLIVVSFMTLLFCVKVKKDIAVLSNSDPSLVLAFLLCFAISSISFSFMVSTFFSKANMAATVGGFLYFFTYTPYFFVAPRYNWMTLSQKLLSCLLSNVAMAMGAQLIGKFEAKGTGIQWCDLLNPVNVDDDFCFGQVLGMLLLDSVLYGLVTWYVEAVFPGQFGVPQPWYFFLMPSYWCGNPRTVVGKEEEGGDPEKAFRTEYFEAEPEDLAAGIKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSMLTGLFPPTSGHAYIRGYEISQDMVQIRKSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSVQKCPEEVKQMLHTLGLEDKRDSRSKFLSGGMKRKLAIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSSLFLKQKYGAGYHMTLVKEPHCNPEGISQLVHHHVPNAMLESHAGAELSFILPKESTHRFESLFAKLEKKQKELGIASFGASVTTMEEVFLRVGKLVDTSMDIQAIQLPALQYQHERRASDWALDSNLCGVMDPTNGIGALIEEEEVLVKLNTGLALHCQQFWAMFLKKAAYSWREWRMVAAQILVPVTCLTLALLAINYTSEIFDDPPLKLSLNEYGTTVVPFSVPGTSRLGQQLSEHLRDMLQAERQEPREVLGDLEEFLVFRASVEGGGFNERCLVATSFKDSGERTVVTALFNNQAYHSPATALAIVDNLLFKLLCGPRASIEISNYPQPRSTLQVAKDQFNEGRKGFDIALNLLIAMAFLASTFSILAVSERAVQAKHVQFVSGVHVATFWLSALLWDLISFLVPSLLLLVVFRAFDVHAFTRDGHMADLLLLLMLYGWAIIPLMYLLSFFFSAASTAYTRLTIFNILSGIATFIVVTIMRIPAVKLEELSRTLDHVFLVLPNHCLGMAVSNFYENYETRRYCTSSEVATHYCKKYNIQYQENFYAWSTPGIGKFVTSMAASGGIYLTLLFLIETNLLWRLRTFVCAFRRRWTLAELQNRTSVLPEDQDVADERSRVLVPSLDSMLDTPLIINELSKVYDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGYCPQFDALLDHMTGREMLVMYARLRGIPERLIDACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGSGYSLQAKVRSEGKQEVLEEFKAFVDLTFPGSVLEDEHQDMVHYHLPGCDLSWAKVFGILEKAKEKYGVDDYSVSQISLEQVFLSFAHLQPPTTEDGR | ||||||
Glycosylation | 14 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 53 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 124 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 140 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000452300 | 175-1704 | 150 Kda mature form | |||
Sequence: ETEGWHTASLFPLFPSPGPREPSSPDGGEPGYIREGFLAVQHAVDKAIMHYHANASAHQLFQKLTVITKRFPFPPYISDPFLIAIQYQLPLLLMLSFTYTSLTIIRAVVQEKEKKLKEYMRMMGLSSWLHWSAWFLMFLLFSLIVVSFMTLLFCVKVKKDIAVLSNSDPSLVLAFLLCFAISSISFSFMVSTFFSKANMAATVGGFLYFFTYTPYFFVAPRYNWMTLSQKLLSCLLSNVAMAMGAQLIGKFEAKGTGIQWCDLLNPVNVDDDFCFGQVLGMLLLDSVLYGLVTWYVEAVFPGQFGVPQPWYFFLMPSYWCGNPRTVVGKEEEGGDPEKAFRTEYFEAEPEDLAAGIKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSMLTGLFPPTSGHAYIRGYEISQDMVQIRKSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSVQKCPEEVKQMLHTLGLEDKRDSRSKFLSGGMKRKLAIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSSLFLKQKYGAGYHMTLVKEPHCNPEGISQLVHHHVPNAMLESHAGAELSFILPKESTHRFESLFAKLEKKQKELGIASFGASVTTMEEVFLRVGKLVDTSMDIQAIQLPALQYQHERRASDWALDSNLCGVMDPTNGIGALIEEEEVLVKLNTGLALHCQQFWAMFLKKAAYSWREWRMVAAQILVPVTCLTLALLAINYTSEIFDDPPLKLSLNEYGTTVVPFSVPGTSRLGQQLSEHLRDMLQAERQEPREVLGDLEEFLVFRASVEGGGFNERCLVATSFKDSGERTVVTALFNNQAYHSPATALAIVDNLLFKLLCGPRASIEISNYPQPRSTLQVAKDQFNEGRKGFDIALNLLIAMAFLASTFSILAVSERAVQAKHVQFVSGVHVATFWLSALLWDLISFLVPSLLLLVVFRAFDVHAFTRDGHMADLLLLLMLYGWAIIPLMYLLSFFFSAASTAYTRLTIFNILSGIATFIVVTIMRIPAVKLEELSRTLDHVFLVLPNHCLGMAVSNFYENYETRRYCTSSEVATHYCKKYNIQYQENFYAWSTPGIGKFVTSMAASGGIYLTLLFLIETNLLWRLRTFVCAFRRRWTLAELQNRTSVLPEDQDVADERSRVLVPSLDSMLDTPLIINELSKVYDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGYCPQFDALLDHMTGREMLVMYARLRGIPERLIDACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGSGYSLQAKVRSEGKQEVLEEFKAFVDLTFPGSVLEDEHQDMVHYHLPGCDLSWAKVFGILEKAKEKYGVDDYSVSQISLEQVFLSFAHLQPPTTEDGR | ||||||
Glycosylation | 228 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 620 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 945 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1350 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated. Localization at intracellular vesicles is accompanied by processing of oligosaccharide from high mannose type to complex type. N-linked glycosylation at Asn-124 and Asn-140 is required for stability and efficient anterograde trafficking and prevents from proteasomal degradation.
Proteolytically cleaved by CTSL and to a lower extent by CTSB within multivesicular bodies (MVB) and lamellar bodies (LB) leading to a mature form of 150 kDa.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in lung, moderately expressed in stomach, intestine, and kidney and weakly expressed in thyroid, brain, liver, spleen, heart, testis, and thymus.
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 530-763 | ABC transporter 1 | ||||
Sequence: IKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSMLTGLFPPTSGHAYIRGYEISQDMVQIRKSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSVQKCPEEVKQMLHTLGLEDKRDSRSKFLSGGMKRKLAIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSSLFLKQKYGAGYHMTLV | ||||||
Domain | 1381-1614 | ABC transporter 2 | ||||
Sequence: LIINELSKVYDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGYCPQFDALLDHMTGREMLVMYARLRGIPERLIDACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGSGYSLQAK |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,704
- Mass (Da)191,767
- Last updated2015-07-22 v1
- ChecksumA1F47B43E9CEB8CC
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AIR0 | A0A8I6AIR0_RAT | Abca3 | 1686 | ||
A0A8I6AQZ2 | A0A8I6AQZ2_RAT | Abca3 | 1449 | ||
Q5M866 | Q5M866_RAT | Abca3 | 152 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC098526 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC103090 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |